CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001639
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Bromodomain-containing protein 1 
Protein Synonyms/Alias
 BR140-like protein; Bromodomain and PHD finger-containing protein 2 
Gene Name
 BRD1 
Gene Synonyms/Alias
 BRL; BRPF2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
368YMKMEPVKELTGGGTacetylation[1]
368YMKMEPVKELTGGGTubiquitination[2]
418CRKESSVKTVRSTSKacetylation[1]
516RENDEEMKAAKEKLKacetylation[1]
519DEEMKAAKEKLKYWQacetylation[1]
523KAAKEKLKYWQRLRHacetylation[1]
903IENGNYAKAARIAAEacetylation[1]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473] 
Functional Description
 Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. 
Sequence Annotation
 DOMAIN 579 649 Bromo.
 DOMAIN 929 1012 PWWP.
 ZN_FING 214 264 PHD-type.
 MOD_RES 128 128 Phosphoserine.
 MOD_RES 368 368 N6-acetyllysine.
 MOD_RES 516 516 N6-acetyllysine.
 MOD_RES 519 519 N6-acetyllysine.
 MOD_RES 903 903 N6-acetyllysine.
 MOD_RES 1052 1052 Phosphoserine.
 MOD_RES 1055 1055 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Bromodomain; Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1058 AA 
Protein Sequence
MRRKGRCHRG SAARHPSSPC SVKHSPTRET LTYAQAQRMV EIEIEGRLHR ISIFDPLEII 60
LEDDLTAQEM SECNSNKENS ERPPVCLRTK RHKNNRVKKK NEALPSAHGT PASASALPEP 120
KVRIVEYSPP SAPRRPPVYY KFIEKSAEEL DNEVEYDMDE EDYAWLEIVN EKRKGDCVPA 180
VSQSMFEFLM DRFEKESHCE NQKQGEQQSL IDEDAVCCIC MDGECQNSNV ILFCDMCNLA 240
VHQECYGVPY IPEGQWLCRH CLQSRARPAD CVLCPNKGGA FKKTDDDRWG HVVCALWIPE 300
VGFANTVFIE PIDGVRNIPP ARWKLTCYLC KQKGVGACIQ CHKANCYTAF HVTCAQKAGL 360
YMKMEPVKEL TGGGTTFSVR KTAYCDVHTP PGCTRRPLNI YGDVEMKNGV CRKESSVKTV 420
RSTSKVRKKA KKAKKALAEP CAVLPTVCAP YIPPQRLNRI ANQVAIQRKK QFVERAHSYW 480
LLKRLSRNGA PLLRRLQSSL QSQRSSQQRE NDEEMKAAKE KLKYWQRLRH DLERARLLIE 540
LLRKREKLKR EQVKVEQVAM ELRLTPLTVL LRSVLDQLQD KDPARIFAQP VSLKEVPDYL 600
DHIKHPMDFA TMRKRLEAQG YKNLHEFEED FDLIIDNCMK YNARDTVFYR AAVRLRDQGG 660
VVLRQARREV DSIGLEEASG MHLPERPAAA PRRPFSWEDV DRLLDPANRA HLGLEEQLRE 720
LLDMLDLTCA MKSSGSRSKR AKLLKKEIAL LRNKLSQQHS QPLPTGPGLE GFEEDGAALG 780
PEAGEEVLPR LETLLQPRKR SRSTCGDSEV EEESPGKRLD AGLTNGFGGA RSEQEPGGGL 840
GRKATPRRRC ASESSISSSN SPLCDSSFNA PKCGRGKPAL VRRHTLEDRS ELISCIENGN 900
YAKAARIAAE VGQSSMWIST DAAASVLEPL KVVWAKCSGY PSYPALIIDP KMPRVPGHHN 960
GVTIPAPPLD VLKIGEHMQT KSDEKLFLVL FFDNKRSWQW LPKSKMVPLG IDETIDKLKM 1020
MEGRNSSIRK AVRIAFDRAM NHLSRVHGEP TSDLSDID 1058 
Gene Ontology
 GO:0070776; C:MOZ/MORF histone acetyltransferase complex; IDA:UniProtKB.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0043966; P:histone H3 acetylation; IDA:UniProtKB. 
Interpro
 IPR001487; Bromodomain.
 IPR018359; Bromodomain_CS.
 IPR019542; Enhancer_polycomb-like_N.
 IPR000313; PWWP.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF10513; EPL1
 PF00855; PWWP 
SMART
 SM00297; BROMO
 SM00249; PHD
 SM00293; PWWP 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50812; PWWP
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS
 PR00503; BROMODOMAIN.